{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Miller MR"],"funding":["NIDCR NIH HHS","NCRR NIH HHS","NIAID NIH HHS","NIGMS NIH HHS","NIH HHS","Intramural CDC HHS"],"pagination":["16134"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC5077173"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["1(10)"],"pubmed_abstract":["Spirochaetes are bacteria responsible for several serious diseases, including Lyme disease (Borrelia burgdorferi), syphilis (Treponema pallidum) and leptospirosis (Leptospira interrogans), and contribute to periodontal diseases (Treponema denticola)(1). These spirochaetes employ an unusual form of flagella-based motility necessary for pathogenicity; indeed, spirochaete flagella (periplasmic flagella) reside and rotate within the periplasmic space(2-11). The universal joint or hook that links the rotary motor to the filament is composed of ∼120-130 FlgE proteins, which in spirochaetes form an unusually stable, high-molecular-weight complex(9,12-17). In other bacteria, the hook can be readily dissociated by treatments such as heat(18). In contrast, spirochaete hooks are resistant to these tr"],"journal":["Nature microbiology"],"pubmed_title":["Spirochaete flagella hook proteins self-catalyse a lysinoalanine covalent crosslink for motility."],"pmcid":["PMC5077173"],"funding_grant_id":["R01 DE023080","R01 AI078958","CC999999","S10 OD017992","S10 RR025449","P41 GM103485","T32 DE023526","R01 DE023431","R01 GM064664","R01 AI087946","R21 DE023432"],"pubmed_authors":["Liu J","Charon NW","James ME","Li C","Bian J","Callery PS","Zhang S","Miller KA","Cockburn A","Crane BR","Lynch MJ","Miller MR","Hettick JM"],"additional_accession":[]},"is_claimable":false,"name":"Spirochaete flagella hook proteins self-catalyse a lysinoalanine covalent crosslink for motility.","description":"Spirochaetes are bacteria responsible for several serious diseases, including Lyme disease (Borrelia burgdorferi), syphilis (Treponema pallidum) and leptospirosis (Leptospira interrogans), and contribute to periodontal diseases (Treponema denticola)(1). These spirochaetes employ an unusual form of flagella-based motility necessary for pathogenicity; indeed, spirochaete flagella (periplasmic flagella) reside and rotate within the periplasmic space(2-11). The universal joint or hook that links the rotary motor to the filament is composed of ∼120-130 FlgE proteins, which in spirochaetes form an unusually stable, high-molecular-weight complex(9,12-17). In other bacteria, the hook can be readily dissociated by treatments such as heat(18). In contrast, spirochaete hooks are resistant to these tr","dates":{"release":"2016-01-01T00:00:00Z","publication":"2016 Aug","modification":"2026-04-14T17:06:49.626Z","creation":"2019-03-27T02:27:23Z"},"accession":"S-EPMC5077173","cross_references":{"pubmed":["27670115"],"doi":["10.1038/nmicrobiol.2016.134"]}}